比较 Hsp70 伴侣蛋白 DnaK 和 BiP 的功能特性。
Comparing the functional properties of the Hsp70 chaperones, DnaK and BiP.
机构信息
Department of Chemical Engineering, Stanford University, 381 North-South Mall, Stanford, CA 94305-5025, USA.
出版信息
Biophys Chem. 2010 Jun;149(1-2):58-66. doi: 10.1016/j.bpc.2010.04.001. Epub 2010 Apr 10.
Abstract
The Hsp70 family of molecular chaperones is an essential class of chaperones that is present in many different cell types and cellular compartments. We have compared the bioactivities of the prokaryotic cytosolic Hsp70, DnaK, to that of the eukaryotic Hsp70, BiP, located in the endoplasmic reticulum (ER). Both chaperones helped to prevent protein aggregation. However, only DnaK provided enhanced refolding of denatured proteins. We also tested chaperone folding assistance during translation in the context of cell-free protein synthesis reactions for several protein targets and show that both DnaK and BiP can provide folding assistance under these conditions. Our results support previous reports suggesting that DnaK provides both post-translational and co-translational folding assistance while BiP predominantly provides folding assistance that is contemporaneous with translation.
摘要
热休克蛋白 70 家族是分子伴侣的重要组成部分，存在于许多不同的细胞类型和细胞区室中。我们比较了原核细胞质 Hsp70，DnaK，和位于内质网 (ER) 中的真核 Hsp70，BiP 的生物活性。两种伴侣蛋白都有助于防止蛋白质聚集。然而，只有 DnaK 提供了变性蛋白的增强重折叠。我们还在无细胞蛋白合成反应中针对几个蛋白靶标测试了伴侣蛋白在翻译过程中的折叠辅助作用，并表明 DnaK 和 BiP 都可以在这些条件下提供折叠辅助。我们的结果支持了先前的报告，表明 DnaK 提供了翻译后和共翻译折叠辅助，而 BiP 主要提供与翻译同时发生的折叠辅助。
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